2JW1

Structural characterization of the type III pilotin-secretin interaction in Shigella flexneri by NMR spectroscopy

2JW1 の概要

• エントリーDOI: 10.2210/pdb2jw1/pdb
• NMR情報: BMRB: 15504
• 分子名称: Lipoprotein mxiM, Outer membrane protein mxiD (2 entities in total)
• 機能のキーワード: protein-protein interaction, lipoprotein, membrane, outer membrane, palmitate, plasmid, virulence, protein transport, transport, membrane protein
• 由来する生物種: Shigella flexneri; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15035.20

構造登録者

Okon, M.S.,Lario, P.I.,Creagh, L.,Jung, Y.M.T.,Maurelli, A.T.,Strynadka, N.C.J.,McIntosh, L.P. (登録日: 2007-10-02, 公開日: 2008-09-02, 最終更新日: 2020-02-19)

主引用文献

Okon, M.,Moraes, T.F.,Lario, P.I.,Creagh, A.L.,Haynes, C.A.,Strynadka, N.C.,McIntosh, L.P.
Structural Characterization of the Type-III Pilot-Secretin Complex from Shigella flexneri
Structure, 16:1544-1554, 2008

PubMed Abstract: Assembly of the type-III secretion apparatus, which translocates proteins through both membranes of Gram-negative bacterial pathogens into host cells, requires the formation of an integral outer-membrane secretin ring. Typically, a small lipidated pilot protein is necessary for the stabilization and localization of this ring. Using NMR spectroscopy, we demonstrate that the C-terminal residues 553-570 of the Shigella flexneri secretin MxiD encompass the minimal binding domain for its cognate pilot MxiM. Although unstructured in isolation, upon complex formation with MxiM, these residues fold into an amphipathic turn-helix motif that caps the elongated hydrophobic cavity of the cracked beta-barrel pilot. Along with a rearrangement of core aromatic residues, this prevents the binding of lipids within the cavity. The mutually exclusive association of lipids and MxiD with MxiM establishes a framework for understanding the role of a pilot in the outer-membrane insertion and multimerization of the secretin ring.

PubMed: 18940609
DOI: 10.1016/j.str.2008.08.006

実験手法

SOLUTION NMR